Glutathione S-transferase class-mu 26 kDa isozyme - Schistosoma japonicum (Blood fluke)

Contribute

Send feedback

Read comments (?) or add your own

P08515 (GST26_SCHJA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 27, 2011. Version 89. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names	Recommended name: Glutathione S-transferase class-mu 26 kDa isozyme Short name=GST 26 EC=2.5.1.18 Alternative name(s): Sj26 antigen SjGST
Organism	Schistosoma japonicum (Blood fluke)
Taxonomic identifier	6182 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Platyhelminthes › Trematoda › Digenea › Strigeidida › Schistosomatoidea › Schistosomatidae › Schistosoma

Protein attributes

Sequence length	218 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut.
Catalytic activity	RX + glutathione = HX + R-S-glutathione.
Subunit structure	Homodimer.
Miscellaneous	There are at least two isoenzymes of GST in S.japonicum.
Sequence similarities	Belongs to the GST superfamily. Mu family. Contains 1 GST C-terminal domain. Contains 1 GST N-terminal domain.

Ontologies

Keywords
Molecular function	Transferase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Molecular function	glutathione transferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.3

Chain

2 – 218

217

Glutathione S-transferase class-mu 26 kDa isozyme

PRO_0000185805

Regions

Domain

2 – 83

GST N-terminal

Domain

85 – 203

119

GST C-terminal

Region

7 – 8

Glutathione binding

Region

41 – 45

Glutathione binding

Region

54 – 55

Glutathione binding

Region

67 – 68

Glutathione binding

Sites

Binding site

111

Substrate Probable

Secondary structure

218

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P08515 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 5E2AC418BD0EF13F
Show »

FASTA

218

25,499

        10         20         30         40         50         60 
MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID 

        70         80         90        100        110        120 
GDVKLTQSMA IIRYIADKHN MLGGCPKERA EISMLEGAVL DIRYGVSRIA YSKDFETLKV 

       130        140        150        160        170        180 
DFLSKLPEML KMFEDRLCHK TYLNGDHVTH PDFMLYDALD VVLYMDPMCL DAFPKLVCFK 

       190        200        210 
KRIEAIPQID KYLKSSKYIA WPLQGWQATF GGGDHPPK

« Hide

References

[1]	"Mr 26,000 antigen of Schistosoma japonicum recognized by resistant WEHI 129/J mice is a parasite glutathione S-transferase." Smith D.B., Davern K.M., Board P.G., Tiu W.U., Garcia E.G., Mitchell G.F. Proc. Natl. Acad. Sci. U.S.A. 83:8703-8707(1986) [PubMed: 3095841] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	Smith D.B., Davern K.M., Board P.G., Tiu W.U., Garcia E.G., Mitchell G.F. Proc. Natl. Acad. Sci. U.S.A. 84:6541-6541(1987) Cited for: SEQUENCE REVISION.
[3]	"Expression of an enzymatically active parasite molecule in Escherichia coli: Schistosoma japonicum glutathione S-transferase." Smith D.B., Rubira M.R., Simpson R.J., Davern K.M., Tiu W.U., Board P.G., Mitchell G.F. Mol. Biochem. Parasitol. 27:249-256(1988) [PubMed: 3278228] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-15.
[4]	"Three-dimensional structure of Schistosoma japonicum glutathione S-transferase fused with a six-amino acid conserved neutralizing epitope of gp41 from HIV." Lim K., Ho J.X., Keeling K., Gilliland G.L., Ji X., Ruker F., Carter D.C. Protein Sci. 3:2233-2244(1994) [PubMed: 7538846] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[5]	"Crystal structures of a schistosomal drug and vaccine target: glutathione S-transferase from Schistosoma japonica and its complex with the leading antischistosomal drug praziquantel." McTigue M.A., Williams D.R., Tainer J.A. J. Mol. Biol. 246:21-27(1995) [PubMed: 7853399] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH INHIBITOR PRAZIQUANTEL.
[6]	"Characterization of the electrophile binding site and substrate binding mode of the 26-kDa glutathione S-transferase from Schistosoma japonicum." Cardoso R.M., Daniels D.S., Bruns C.M., Tainer J.A. Proteins 51:137-146(2003) [PubMed: 12596270] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH GLUTATHIONE ANALOGS.
[7]	"Using affinity chromatography to engineer and characterize pH-dependent protein switches." Sagermann M., Chapleau R.R., DeLorimier E., Lei M. Protein Sci. 18:217-228(2009) [PubMed: 19177365] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-214.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M14654 mRNA. Translation: AAB59203.1.

PIR

A61514.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B8X	X-ray	2.70	A	2-218	[»]
1BG5	X-ray	2.60	A	1-218	[»]
1DUG	X-ray	1.80	A/B	2-218	[»]
1GNE	X-ray	2.50	A	1-218	[»]
1GTA	X-ray	2.40	A	1-218	[»]
1GTB	X-ray	2.60	A	1-218	[»]
1M99	X-ray	2.30	A	1-218	[»]
1M9A	X-ray	2.10	A	1-218	[»]
1M9B	X-ray	2.60	A	1-218	[»]
1U87	X-ray	3.50	A	1-218	[»]
1U88	X-ray	3.50	A/B	1-218	[»]
1UA5	X-ray	2.50	A	1-218	[»]
1Y6E	X-ray	3.00	A/B	2-217	[»]
3CRT	X-ray	1.90	A	1-214	[»]
3CRU	X-ray	2.30	A	1-214	[»]
3D0Z	X-ray	2.50	A	1-214	[»]
3QMZ	X-ray	6.00	S/T	2-218	[»]

ProteinModelPortal

P08515.

SMR

P08515. Positions 2-218.

ModBase

Search...

Protein-protein interaction databases

STRING

P08515.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

Gene3D

G3DSA:1.20.1050.10. GST_C_like. 1 hit.
G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.

Pfam

PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]

SUPFAM

SSF47616. GST_C_like. 1 hit.
SSF52833. Thiordxn-like_fd. 1 hit.

PROSITE

PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00143. Glutathione.
DB01058. Praziquantel.

Entry information

Entry name

GST26_SCHJA

Accession

Primary (citable) accession number: P08515

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	January 23, 2007
Last modified:	July 27, 2011
This is version 89 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Family and domain databases

Other

Entry information

Relevant documents